Beauvais A, Monod M, Wyniger J, Debeaupuis J P, Grouzmann E, Brakch N, Svab J, Hovanessian A G, Latgé J P
Laboratoire des Aspergillus, Institut Pasteur, Paris, France.
Infect Immun. 1997 Aug;65(8):3042-7. doi: 10.1128/iai.65.8.3042-3047.1997.
A dipeptidyl-peptidase IV was purified from the culture medium of the human-pathogenic fungus Aspergillus fumigatus. The enzyme has an apparent molecular mass of 95 kDa and contained approximately 10 kDa of N-linked carbohydrate. This glycoprotein is antigenic and has all characteristics of the class IV dipeptidyl-peptidases: removal of Xaa-Pro and to a lesser extent Xaa-Ala dipeptides from the N termini of peptides, including bioactive peptides such as neuropeptide Y, [des-Arg1] bradykinin, and glucagon-like peptide 1, activity at neutral pH, and presence in the amino acid sequence of the Gly-X-Ser-X-Gly consensus motif of the serine-hydrolases and the putative catalytic triad (Ser613, Asp690, His725) of the dipeptidyl-peptidases. Moreover, the last 200 amino acids displayed 60 to 65% similarity with the other dipeptidyl-peptidases IV from rat, mouse, human, and yeast. However, unlike the other dipeptidyl-peptidases, the dipeptidyl-peptidase IV of A. fumigatus is a secreted enzyme with a cleavable signal peptide. Expression of a recombinant dipeptidyl-peptidase IV of A. fumigatus has been attained in the yeast Pichia pastoris.
从人类致病真菌烟曲霉的培养基中纯化出一种二肽基肽酶IV。该酶的表观分子量为95 kDa，含有约10 kDa的N-连接碳水化合物。这种糖蛋白具有抗原性，具备IV类二肽基肽酶的所有特征：从肽的N端去除Xaa-Pro以及在较小程度上去除Xaa-Ala二肽，包括生物活性肽如神经肽Y、[去-Arg1]缓激肽和胰高血糖素样肽1；在中性pH下具有活性；存在于丝氨酸水解酶的Gly-X-Ser-X-Gly共有基序的氨基酸序列以及二肽基肽酶的假定催化三联体（Ser613、Asp690、His725）中。此外，其最后200个氨基酸与大鼠、小鼠、人类和酵母的其他二肽基肽酶IV显示出60%至65%的相似性。然而，与其他二肽基肽酶不同的是，烟曲霉的二肽基肽酶IV是一种具有可裂解信号肽的分泌酶。烟曲霉重组二肽基肽酶IV已在毕赤酵母中实现表达。
